AMYB_TRIRP
ID AMYB_TRIRP Reviewed; 496 AA.
AC O65015;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Beta-amylase;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
GN Name=BMY1;
OS Trifolium repens (Creeping white clover).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX NCBI_TaxID=3899;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gallagher J., Gana J.A., Pollock C., Cunningham S.M., Volenec J.J.;
RT "Nucleotide sequence of a beta-amylase cDNA from white clover stollons.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides so as to remove successive maltose units from the
CC non-reducing ends of the chains.; EC=3.2.1.2;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
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DR EMBL; AF049098; AAD04259.1; -; mRNA.
DR PIR; T08117; T08117.
DR AlphaFoldDB; O65015; -.
DR SMR; O65015; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001554; Glyco_hydro_14.
DR InterPro; IPR018238; Glyco_hydro_14_CS.
DR InterPro; IPR001371; Glyco_hydro_14B_pln.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352; PTHR31352; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation.
FT CHAIN 1..496
FT /note="Beta-amylase"
FT /id="PRO_0000153939"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 382..383
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
SQ SEQUENCE 496 AA; 56088 MW; 8FC446AB7C927F19 CRC64;
MATSNKNMLL NYVPVYVMLP LGVINVNNVF EDPDGLKEQL VQLRAAGVDG VMVDVWWGII
EQKGPKEYDW SAYKSLFQLV QECGLKLQAI MSFHQCGGNV GDVVTIPIPQ WVLDIGESDP
DIFYTNRSGT RDKEYLTVGV DNKPIFHGRT AIEIYSDYMK SFRENMSEFL KSELIIDIEV
GLGPAGELRY PSYPQNQGWV FPGIGEFQCY DKYLKADFKA AAAKAGHSEW ELPDDAGTYN
DIPESTEFFK TNGTYLTEKG KFFLTWYSNQ LLNHGDQILD EANKAFLGCK VKLAIKVSGI
HWWYKAQNHA AELTAGYYNL DDRDGYRPIA KMVSRHHGIL NFTCLEMRDS EQSSDAQSAP
QELVQQVLSG GWRENIEVAG ENALSRYDAT AYNQIILNAR PQGVNKDGPP KLRMYGVTYL
RLSDDLLQES NFEIFKKFVV KMHADQSHCD DPQEYNHAIP PLKRSGPNIP VDDLLEATKP
ILPFPWDSET DMKVDG
